Engineering a naturally inactive isoform of type III antifreeze protein into one that can stop the growth of ice

Garnham, Christopher P.; Nishimiya, Yoshiyuki; Tsuda, Sakae; Davies, Peter L.

doi:10.1016/j.febslet.2012.09.017

Cited by 28 publications

(38 citation statements)

References 30 publications

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“…). A previous study revealed that replacement of these four residues in nfeAFP11 with the corresponding residues of the QAE1 isoform converted the inactive isoform into a fully active AFP (called QAE1‐like AFP) . This study further found that the triple mutant of nfeAFP11 (V9Q/V19L/G20V) also showed significant TH activity .…”

Section: Discussionsupporting

confidence: 57%

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NMR study of the antifreeze activities of active and inactive isoforms of a type III antifreeze protein

et al. 2016

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The quaternary-amino-ethyl 1 (QAE1) isoforms of type III antifreeze proteins (AFPs) prevent the growth of ice crystals within organisms living in polar regions. We determined the antifreeze activity of wild-type and mutant constructs of the Japanese notched-fin eelpout (Zoarces elongates Kner) AFP8 (nfeAFP8) and characterized the structural and dynamics properties of their ice-binding surface using NMR. We found that the three constructs containing the V20G mutation were incapable of stopping the growth of ice crystals and exhibited structural changes, as well as increased conformational flexibility, in the first 3 helix (residues 18-22) of the sequence. Our results suggest that the inactive nfeAFP8s are incapable of anchoring water molecules due to the unusual and flexible backbone conformation of their primary prism plane-binding surface.

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Section: Discussionsupporting

confidence: 57%

“…Previous studies also reported that this T18‐Hγ1 resonance was observed in the active mutant of nfeAFP11 (V9Q/V19L/G20V), suggesting the presence of a stable H‐bond between T18‐Hγ1 and a water molecule (Fig. C) . However, like wt nfeAFP11 , the inactive nfeAFP8s did not show these resonances (Fig.…”

Section: Discussionmentioning

confidence: 59%

NMR study of the antifreeze activities of active and inactive isoforms of a type III antifreeze protein

et al. 2016

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“…While the QAE1 isoform is able to bind both the primary prism and a pyramidal plane of ice, the SP and QAE2 isoforms can only bind pyramidal ice planes [134]. Interestingly, a triple mutant of the inactive QAE2 isoform (V9Q/V19L/G20V) is able to bind to the primary prism ice plane and shows full TH activity, similar to the QAE1 isoform [135]. More recently, NMR experiments with inactive QAE2-like mutants containing the V20G mutation were reported.…”

Section: Marine-derived Afpsmentioning

confidence: 99%

Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant

et al. 2017

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Antifreeze proteins (AFPs) are biological antifreezes with unique properties, including thermal hysteresis (TH), ice recrystallization inhibition (IRI), and interaction with membranes and/or membrane proteins. These properties have been utilized in the preservation of biological samples at low temperatures. Here, we review the structure and function of marine-derived AFPs, including moderately active fish AFPs and hyperactive polar AFPs. We also survey previous and current reports of cryopreservation using AFPs. Cryopreserved biological samples are relatively diverse ranging from diatoms and reproductive cells to embryos and organs. Cryopreserved biological samples mainly originate from mammals. Most cryopreservation trials using marine-derived AFPs have demonstrated that addition of AFPs can improve post-thaw viability regardless of freezing method (slow-freezing or vitrification), storage temperature, and types of biological sample type.

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“…Ice crystal controlling activity is affected to a significant extent by solvent exposed amino acid residues that are found along the ice-binding surface. By changing theses residues to match one of the ice crystal planes, inactive antifreeze protein isoforms can be altered to be active [73]. Consequently, solvent exposed residues play a major role in ice crystal interaction.…”

Section: Biochemistrymentioning

confidence: 99%

Bacterial Ice Crystal Controlling Proteins

2014

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Across the world, many ice active bacteria utilize ice crystal controlling proteins for aid in freezing tolerance at subzero temperatures. Ice crystal controlling proteins include both antifreeze and ice nucleation proteins. Antifreeze proteins minimize freezing damage by inhibiting growth of large ice crystals, while ice nucleation proteins induce formation of embryonic ice crystals. Although both protein classes have differing functions, these proteins use the same ice binding mechanisms. Rather than direct binding, it is probable that these protein classes create an ice surface prior to ice crystal surface adsorption. Function is differentiated by molecular size of the protein. This paper reviews the similar and different aspects of bacterial antifreeze and ice nucleation proteins, the role of these proteins in freezing tolerance, prevalence of these proteins in psychrophiles, and current mechanisms of protein-ice interactions.

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Engineering a naturally inactive isoform of type III antifreeze protein into one that can stop the growth of ice

Cited by 28 publications

References 30 publications

NMR study of the antifreeze activities of active and inactive isoforms of a type III antifreeze protein

NMR study of the antifreeze activities of active and inactive isoforms of a type III antifreeze protein

Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant

Bacterial Ice Crystal Controlling Proteins

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